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首页> 外文期刊>The Journal of Experimental Biology >The neuropeptide proctolin induces phosphorylation of a 30 kDa proteinassociated with the thin filament in crustacean muscle
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The neuropeptide proctolin induces phosphorylation of a 30 kDa proteinassociated with the thin filament in crustacean muscle

机译:神经肽直肠蛋白可诱导30 kDa的蛋白质与甲壳动物肌肉细丝相关的磷酸化

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摘要

In the isopod Idotea emarginata, the neuropeptide proctolin is contained in a single pair of motoneurones located in pereion ganglion 4. The two neurones supply dorsal extensor muscle fibres of all segments. Proctolin (1 mu mol l(-1)) potentiates the amplitude of contractures of single extensor muscle fibres elicited by 10 mmol l(-1) caffeine. In western blots of myofibrillar proteins isolated from single muscle fibres and treated with an antiphosphoserine antibody, a protein with an apparent molecular mass of 30 kDa was consistently found. The phosphorylation of this protein was significantly increased by treating the fibres with proctolin. After separation of myofibrillar filaments, a 30 kDa protein was found only in the thin filament fraction. This protein is phosphorylated and detected by an antiserum against crustacean troponin 1.
机译:在等足线虫Idotea emarginata中,神经肽的促泌素蛋白包含在位于小神经节4中的一对运动神经元中。这两个神经元提供所有节段的背伸肌纤维。 Proctolin(1μmol l(-1))增强了10 mmol l(-1)咖啡因引起的单个伸肌纤维挛缩的幅度。在从单条肌纤维分离并用抗磷酸丝氨酸抗体处理的肌原纤维蛋白的蛋白质印迹中,一致地发现了一种表观分子量为30 kDa的蛋白。该蛋白的磷酸化通过用蛋白凝蛋白处理纤维而显着增加。分离肌原纤维细丝后,仅在细丝部分中发现了30 kDa的蛋白质。该蛋白质被磷酸化,并通过抗甲壳类肌钙蛋白1的抗血清进行检测。

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